August 2017 | Volume 149, No. 8

Cover image

Cover picture: Structures of a GIRK2 channel following molecular dynamics simulations show a closed state for the wild-type channel and a hypothetical open state for a mutant K200Y (KY) channel. Cross-sectional views (right) highlight the transmembrane gate (green) in the pore and PIP2. The authors provide evidence that the KY mutation in the PIP2-binding pocket leads to channel activation (see Research Article by Lacin et al., 799–811).